Purification and characterization of an intracellular heat-stable proteinase (pernilase) from the marine hyperthermophilic archaeon Aeropyrum pernix K1

Extremophiles ◽  
1999 ◽  
Vol 3 (1) ◽  
pp. 3-9 ◽  
Author(s):  
Pamela Chavez Croocker ◽  
Y. Sako ◽  
Aritsune Uchida
Keyword(s):  
Purification And Characterization ◽  
Hyperthermophilic Archaeon ◽  
Aeropyrum Pernix ◽  
Heat Stable

Purification and characterization of carbon monoxide dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix

2010 ◽  
Vol 76 (6) ◽  
pp. 999-1006 ◽  
Author(s):  
Hiroshi Nishimura ◽  
Yoshiko Nomura ◽  
Eri Iwata ◽  
Nozomi Sato ◽  
Yoshihiko Sako
Keyword(s):  
Carbon Monoxide ◽  
Carbon Monoxide Dehydrogenase ◽  
Purification And Characterization ◽  
Hyperthermophilic Archaeon ◽  
Aeropyrum Pernix

scholarly journals Purification and characterization of the heat-stable serine proteinase from Thermomonospora fusca YX

1987 ◽  
Vol 246 (2) ◽  
pp. 511-517 ◽  
Author(s):  
T W Gusek ◽  
J E Kinsella
Keyword(s):  
Thermal Stability ◽  
Ionic Strength ◽  
Serine Proteinase ◽  
Maximum Activity ◽  
Exchange Chromatography ◽  
Cation Exchange Chromatography ◽  
Purification And Characterization ◽  
Thermomonospora Fusca ◽  
Heat Stable

The proteinase secreted from Thermomonospora fusca YX grown on cellulose was purified by (NH4)2SO4 fractionation and cation-exchange chromatography. The isolated proteinase readily hydrolysed several proteins and demonstrated activity towards casein from 35 to 95 degrees C (at pH 8.0) with maximum activity at 80 degrees C. It exhibited broad pH and ionic-strength optima centered at pH 9.0 and 0.2 M-NaCl respectively, and it retained high activity in the presence of 2% (w/v) SDS, 20 mM-dithiothreitol and 1.0 M-NaCl. The proteinase, which was fully inhibited by phenylmethanesulphonyl fluoride, had an Mr of 14,500 and an isoelectric point at 9.21. A measurement of proteinase thermal stability demonstrated a T50% (15 min) of 85 degrees C at pH 4.5.

scholarly journals Characterization of a heat-stable enzyme possessing GTP-dependent RNA ligase activity from a hyperthermophilic archaeon, Pyrococcus furiosus

RNA ◽  
2009 ◽  
Vol 15 (3) ◽  
pp. 420-431 ◽  
Author(s):  
A. Kanai ◽  
A. Sato ◽  
Y. Fukuda ◽  
K. Okada ◽  
T. Matsuda ◽  
...  
Keyword(s):  
Pyrococcus Furiosus ◽  
Rna Ligase ◽  
Hyperthermophilic Archaeon ◽  
Heat Stable

scholarly journals Purification and characterization of a heat-stable enterotoxin ofVibrio mimicus

1991 ◽  
Vol 79 (1) ◽  
pp. 105-110 ◽  
Author(s):  
Michiko Arita ◽  
Takeshi Honda ◽  
Toshio Miwatani ◽  
Tae Takeda ◽  
Toshifumi Takao ◽  
...  
Keyword(s):  
Purification And Characterization ◽  
Heat Stable
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